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JXB Advance Access originally published online on January 12, 2004
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Journal of Experimental Botany, Vol. 55, No. 396, pp. 377-385, February 1, 2004
© 2004 Oxford University Press

Cell and Molecular Biology, Biochemistry and Molecular Physiology

A novel cDNA from Parthenium argentatum Gray enhances the rubber biosynthetic activity in vitro*

Received 9 June 2003; Accepted 15 October 2003

In Jeong Kim2, Stephen B. Ryu1, Yeon Sig Kwak1 and Hunseung Kang1,2,{dagger}

1 Kumho Life and Environmental Science Laboratory, 1 Oryong-Dong, Buk-Gu, Gwangju, 500-712, Korea
2 Division of Applied Plant Sciences and Agricultural Plant Stress Research Center, College of Agriculture and Life Sciences, Chonnam National University, 300 Yongbong-dong, Buk-gu, Gwangju, 500-757, Korea

* The nucleotide sequence reported in this paper has been deposited in the GenBank database under GenBank accession no. AF541942.
{dagger} To whom correspondence should be addressed. Fax: +82 62 530 2047. E-mail: hskang{at}chonnam.chonnam.ac.kr
Abbreviations: CPT, cis-prenyltransferase; FDP, farnesyl diphosphate; GHS, guayule homologue of SRPP; IDP, isopentenyl diphosphate; PAGE, polyacrylamide gel electrophoresis; SRPP, small rubber particle protein; WRP, washed rubber particle.

Natural rubber (cis-1,4-polyisoprene) is an isoprenoid compound produced exclusively in plants by the action of rubber transferase. Despite a keen interest in revealing the mechanisms of rubber chain elongation and chain length determination, the molecular nature of rubber transferase has not yet been identified. A recent report has revealed that a 24 kDa protein tightly associated with the small rubber particles of Hevea brasiliensis, therefore designated small rubber particle protein (SRPP), plays a positive role in rubber biosynthesis. Since guayule (Parthenium argentatum Gray) produces natural rubber similar in size to H. brasiliensis, it is of critical interest to investigate whether guayule contains a similar protein to the SRPP. A cDNA clone has been isolated in guayule that shares a sequence homology with the SRPP, thus designated guayule homologue of SRPP (GHS), and the catalytic function of the protein was characterized. Sequence analysis revealed that the GHS is highly homologous in several conserved regions to the SRPP (50% identity). In vitro functional analysis of the recombinant protein overexpressed in E. coli revealed that the GHS plays a positive role in isopentenyl diphosphate incorporation into high molecular weight rubbers as SRPP does. These results indicate that guayule and Hevea rubber trees contain a protein that is similar in its amino acid sequence and plays a role in isopentenyl diphosphate incorporation in vitro, implying that it contributes to the enhancement of rubber biosynthetic activity in rubber trees.

Key words: Guayule, Hevea brasiliensis, IDP incorporation, Parthenium argentatum, rubber biosynthesis, rubber particle protein.


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K.-S. Chow, K.-L. Wan, Mohd. N. M. Isa, A. Bahari, S.-H. Tan, K Harikrishna, and H.-Y. Yeang
Insights into rubber biosynthesis from transcriptome analysis of Hevea brasiliensis latex
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